› 4c2z

X-ray diffraction
2.08Å resolution

Human N-myristoyltransferase (NMT1) with Myristoyl-CoA and inhibitor bound

Released:
DOI: 10.2210/pdb4c2z/pdb
PDB entry 4c2z coloured by chain, front view.
PDB entry 4c2z coloured by chain, side view.
PDB entry 4c2z coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Global profiling of co- and post-translationally N-myristoylated proteomes in human cells.
Thinon E, Serwa RA, Broncel M, Brannigan JA, Brassat U, Wright MH, Heal WP, Wilkinson AJ, Mann DJ, Tate EW
Nat Commun 5 4919 (2014)
PMID: 25255805

Function and Biology Details

Reaction catalysed: 
Tetradecanoyl-CoA + an N-terminal-glycyl-[protein] = CoA + an N-terminal-N-tetradecanoylglycyl-[protein]
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151725 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycylpeptide N-tetradecanoyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 410 amino acids
Theoretical weight: 47.61 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P30419 (Residues: 109-496; Coverage: 78%)
Gene names: NMT, NMT1
Sequence domains:
Structure domains: Aminopeptidase

Ligands and Environments


Cofactor: Ligand MYA 2 x MYA
5 bound ligands:
Ligand 646 2 x 646
Ligand MG 2 x MG
Ligand CIT 2 x CIT
Ligand GOL 4 x GOL
Ligand CL 8 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P21212
Unit cell:
a: 78.63Å b: 179.12Å c: 58.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.169 0.238
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

33 review citations

Fatty acylation of proteins: The long and the short of it.
Resh MD. (2016)
32 more

3 mentions without citation

Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).
Salah Ud-Din et al. (2016)
2 more